Evidence map›Paper›PMID 22219026›Full record

ArticleMolecular and cellular biochemistry2012

Expression and role in glycolysis of human ADP-dependent glucokinase.

Susan Richter, Jan P Richter, Sunali Y Mehta, Amanda M Gribble, Andrew J Sutherland-Smith, Kathryn M Stowell, Cristin G Print, Ron S Ronimus, William R Wilson

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Article in Molecular and cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 38 citations in OpenAlex.

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  17. Benserazide, a dopadecarboxylase inhibitor, suppresses tumor growth by targeting hexokinase 2.Journal of experimental & clinical cancer research : CR · 2017
    Article
  18. Article
  19. Article
  20. Immunometabolism in Tuberculosis.Frontiers in immunology · 2016
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Susan RichterAuckland Cancer Society Research Centre, Faculty of Medical and Health Sciences, The University of Auckland, Private Bag, 92019 Auckland, New Zealand.
Jan P Richter
Sunali Y Mehta
Amanda M Gribble
Andrew J Sutherland-Smith
Kathryn M Stowell
Cristin G Print
Ron S Ronimus
William R Wilson
Massey University · NZUniversity of Auckland · NZAgResearch · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel murine enzyme, ADP-dependent glucokinase (ADPGK), has been shown to catalyse glucose phosphorylation using ADP as phosphoryl donor. The ancestral ADPGK gene appears to have been laterally transferred from Archaea early in metazoan evolution, but its biological role has not been established. Here, we undertake an initial investigation of the functional properties of human ADPGK in human tumour cell lines and specifically test the hypothesis that ADPGK might prime glycolysis using ADP under stress conditions such as hypoxia. Recombinant human ADPGK was confirmed to catalyse ADP-dependent glucose phosphorylation in vitro, with an apparent K (M) for glucose of 0.29 mM. Expression databases and western blotting of surgical samples demonstrated high expression in many human tissues, including tumours. Unlike hexokinase-2 (HK2), RNAi studies with exon arrays showed that ADPGK is not a transcriptional target of hypoxia inducible factor-1. Consistent with this, ADPGK protein was not upregulated by hypoxia or anoxia. Surprisingly, stable fivefold overexpression of ADPGK in H460 or HCT116 cells had no apparent effect on proliferation or glycolysis, and did not rescue clonogenicity or glycolysis when HK2 was suppressed by siRNA. Furthermore, suppression of ADPGK by siRNA did not cause detectable inhibition of glycolysis or cell killing by anoxia, although it did induce a statistically significant decrease in plating efficiency of H460 cells under aerobic conditions. Thus, human ADPGK catalyses ADP-dependent phosphorylation of glucose in vitro, but despite its high expression in human tumour cell lines it appears not to make a quantifiable contribution to glycolysis under the conditions evaluated.

Indexed as

GlycolysisAdenosine DiphosphateCatalysisCell HypoxiaCell ProliferationGene Expression Regulation, NeoplasticGlucokinaseGlucoseHCT116 CellsHT29 CellsHumansHypoxia-Inducible Factor 1, alpha SubunitLactic AcidPhosphorylationRecombinant ProteinsRNA, Small InterferingAdenosine DiphosphateADP-dependent glucokinaseGlucokinaseGlucoseHIF1A protein, humanHypoxia-Inducible Factor 1, alpha SubunitLactic AcidRecombinant ProteinsRNA, Small Interfering

Identifiers

PMID22219026
OpenAlexW2090996061

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.